Recombinant expression and anti-microbial activity of anti-lipopolysaccharide factor (ALF) from the black tiger shrimp Penaeus monodon.

[1]  Rath Pichyangkura,et al.  Antimicrobial peptides discovered in the black tiger shrimp Penaeus monodon using the EST approach. , 2004, Diseases of aquatic organisms.

[2]  H. Garay,et al.  Differential regulation of Th1/Th2 in relevant tissues for sepsis pathogenesis with a Limulus anti-LPS factor-derived peptide increases survival in Gram-positive sepsis. , 2004, International immunopharmacology.

[3]  M. Koch,et al.  Cyclic antimicrobial peptides based on Limulus anti-lipopolysaccharide factor for neutralization of lipopolysaccharide. , 2004, Biochemical pharmacology.

[4]  R. Chaby Lipopolysaccharide-binding molecules: transporters, blockers and sensors , 2004, Cellular and Molecular Life Sciences CMLS.

[5]  Y. Guéguen,et al.  Insights into the anti‐microbial defense of marine invertebrates: the penaeid shrimps and the oyster Crassostrea gigas , 2004, Immunological reviews.

[6]  Y. Combarnous,et al.  Overexpression of ovine leptin in Pichia pastoris: physiological yeast response to leptin production and characterization of the recombinant hormone , 2004, Yeast.

[7]  Y. Guéguen,et al.  Involvement of penaeidins in defense reactions of the shrimp Litopenaeus stylirostris to a pathogenic vibrio , 2004, Cellular and Molecular Life Sciences CMLS.

[8]  I. Hirono,et al.  Characterization and function of kuruma shrimp lysozyme possessing lytic activity against Vibrio species. , 2003, Gene.

[9]  M. Almeida,et al.  Production of the active antifungal Pisum sativum defensin 1 (Psd1) in Pichia pastoris: overcoming the inefficiency of the STE13 protease. , 2003, Protein expression and purification.

[10]  M. Finkelman,et al.  Production of recombinant endotoxin neutralizing protein in Pichia pastoris and methods for its purification. , 2002, Protein expression and purification.

[11]  Rath Pichyangkura,et al.  Identification of immune-related genes in hemocytes of black tiger shrimp (Penaeus monodon) , 2002, Marine Biotechnology.

[12]  J. Cregg,et al.  Production of recombinant proteins in fermenter cultures of the yeast Pichia pastoris. , 2002, Current opinion in biotechnology.

[13]  D. Saulnier,et al.  Expression and distribution of penaeidin antimicrobial peptides are regulated by haemocyte reactions in microbial challenged shrimp. , 2002, European journal of biochemistry.

[14]  Guan-Zhen Yang,et al.  Cloning of anti-LPS factor cDNA from Tachypleus tridentatus, expression in Bombyx mori larvae and its biological activity in vitro , 2002, Molecular biotechnology.

[15]  T. Poll Immunotherapy of sepsis , 2001 .

[16]  G. Warr,et al.  Immune gene discovery by expressed sequence tag analysis of hemocytes and hepatopancreas in the Pacific White Shrimp, Litopenaeus vannamei, and the Atlantic White Shrimp, L. setiferus. , 2001, Developmental and comparative immunology.

[17]  Lin Chen,et al.  The Native Gene of Anti-Lps Factor from Tachypleus tridentatus: Cloning, Expression and its Bacteriostatic Activity in Vitro , 2001 .

[18]  B. Hélène,et al.  High-level secretory production of recombinant porcine follicle-stimulating hormone by Pichia pastoris , 2001 .

[19]  C. Goarant,et al.  Experimental infection models for shrimp vibriosis studies: a review , 2000 .

[20]  H. Garay,et al.  A Limulus Antilipopolysaccharide Factor-Derived Peptide Exhibits a New Immunological Activity with Potential Applicability in Infectious Diseases , 2000, Clinical Diagnostic Laboratory Immunology.

[21]  G. Mitta,et al.  Involvement of Mytilins in Mussel Antimicrobial Defense* , 2000, The Journal of Biological Chemistry.

[22]  D. Saulnier,et al.  Rapid and sensitive PCR detection of Vibrio penaeicida, the putative etiological agent of syndrome 93 in New Caledonia. , 2000, Diseases of aquatic organisms.

[23]  A. van Dorsselaer,et al.  Recombinant expression and range of activity of penaeidins, antimicrobial peptides from penaeid shrimp. , 1999, European journal of biochemistry.

[24]  M. Koch,et al.  Biophysical characterisation of lysozyme binding to LPS Re and lipid A. , 1998, European journal of biochemistry.

[25]  J. Schneider-Mergener,et al.  High Affinity Endotoxin-binding and Neutralizing Peptides Based on the Crystal Structure of Recombinant Limulus Anti-lipopolysaccharide Factor* , 1996, The Journal of Biological Chemistry.

[26]  E. Krause,et al.  Peptide helicity and membrane surface charge modulate the balance of electrostatic and hydrophobic interactions with lipid bilayers and biological membranes. , 1996, Biochemistry.

[27]  R. Liddington,et al.  Identification of the LPS-binding domain of an endotoxin neutralising protein, Limulus anti-LPS factor. , 1995, Progress in clinical and biological research.

[28]  K. Muroga,et al.  Vibrio penaeicida sp. nov., a pathogen of kuruma prawns (Penaeus japonicus) , 1995 .

[29]  R. Liddington,et al.  Crystal structure of an endotoxin‐neutralizing protein from the horseshoe crab, Limulus anti‐LPS factor, at 1.5 A resolution. , 1993, The EMBO journal.

[30]  P. Tempst,et al.  Functional and chemical characterization of Hymenoptaecin, an antibacterial polypeptide that is infection-inducible in the honeybee (Apis mellifera). , 1993, The Journal of biological chemistry.

[31]  S. Iwanaga,et al.  The limulus clotting reaction. , 1993, Current opinion in immunology.

[32]  C. Boulin,et al.  Automated multiple peptide synthesis. , 1992, Peptide research.

[33]  R. Potenz,et al.  High-level expression, purification, and characterization of recombinant human tumor necrosis factor synthesized in the methylotrophic yeast Pichia pastoris. , 1989, Biochemistry.

[34]  S. Iwanaga,et al.  PRIMARY STRUCTURE OF ANTI-LIPOPOLYSACCHARIDE FACTOR ISOLATED FROM AMERICAN HORSESHOE CRAB , 1987 .

[35]  S. Iwanaga,et al.  Primary structure of anti-lipopolysaccharide factor from American horseshoe crab, Limulus polyphemus. , 1987, Journal of Biochemistry (Tokyo).

[36]  T. Miyata,et al.  Primary structure of limulus anticoagulant anti-lipopolysaccharide factor. , 1986, The Journal of biological chemistry.

[37]  S. Iwanaga,et al.  Isolation and biological activities of limulus anticoagulant (anti-LPS factor) which interacts with lipopolysaccharide (LPS). , 1985, Journal of biochemistry.

[38]  S. Iwanaga,et al.  Anti‐LPS factor in the horseshoe crab, Tachypleus tridentatus , 1984, FEBS letters.